메뉴 건너뛰기




Volumn 8, Issue 11, 2002, Pages 3527-3538

The cyclin-dependent kinase inhibitor flavopiridol induces apoptosis in multiple myeloma cells through transcriptional repression and down-regulation of Mcl-1

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE INHIBITOR; FLAVOPIRIDOL; MESSENGER RNA; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN MCL 1; RNA POLYMERASE II; BCL2L1 PROTEIN, HUMAN; CASPASE; CYCLIN DEPENDENT KINASE; FLAVONOID; MCL1 PROTEIN; MEMBRANE PROTEIN; PIPERIDINE DERIVATIVE; PROTEIN BCL X; PROTEOGLYCAN; SYNDECAN; TUMOR PROTEIN;

EID: 0036850211     PISSN: 10780432     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (241)

References (86)
  • 2
    • 0031985198 scopus 로고    scopus 로고
    • Multiple myeloma: Increasing evidence for a multistep transformation process
    • Hallek, M., Bergsagel, P. L., and Anderson, K. C. Multiple myeloma: Increasing evidence for a multistep transformation process. Blood, 91: 3-21, 1998.
    • (1998) Blood , vol.91 , pp. 3-21
    • Hallek, M.1    Bergsagel, P.L.2    Anderson, K.C.3
  • 3
    • 0025273433 scopus 로고
    • Oral dosage of melphalan and response to treatment in multiple myeloma
    • Fernberg, J. O., Johansson, B., Lewensohn, R., and Mellstedt, H. Oral dosage of melphalan and response to treatment in multiple myeloma. Eur. J. Cancer, 26: 393-396, 1990.
    • (1990) Eur. J. Cancer , vol.26 , pp. 393-396
    • Fernberg, J.O.1    Johansson, B.2    Lewensohn, R.3    Mellstedt, H.4
  • 4
    • 0026585927 scopus 로고
    • Combination chemotherapy versus melphalan and prednisolone in the treatment of multiple myeloma: An overview of published trials
    • Gregory, W. M., Richards, M. A., and Malpas, J. S. Combination chemotherapy versus melphalan and prednisolone in the treatment of multiple myeloma: An overview of published trials. J. Clin. Oncol., 10: 334-342, 1992.
    • (1992) J. Clin. Oncol. , vol.10 , pp. 334-342
    • Gregory, W.M.1    Richards, M.A.2    Malpas, J.S.3
  • 5
    • 0022655622 scopus 로고
    • High-dose glucocorticoid treatment of resistant myeloma
    • Alexanian, R., Barlogie, B., and Dixon, D. High-dose glucocorticoid treatment of resistant myeloma. Ann. Intern. Med., 105: 8-11, 1986.
    • (1986) Ann. Intern. Med. , vol.105 , pp. 8-11
    • Alexanian, R.1    Barlogie, B.2    Dixon, D.3
  • 6
    • 0025064260 scopus 로고
    • VAD-based regimens as primary treatment for multiple myeloma
    • Alexanian, R., Barlogie, B., and Tucker, S. VAD-based regimens as primary treatment for multiple myeloma. Am. J. Hematol., 33: 86-89, 1990.
    • (1990) Am. J. Hematol. , vol.33 , pp. 86-89
    • Alexanian, R.1    Barlogie, B.2    Tucker, S.3
  • 7
    • 0026656725 scopus 로고
    • Primary dexamethasone treatment of multiple myeloma
    • Alexanian, R., Dimopoulos, M. A., Delasalle, K., and Barlogie, B. Primary dexamethasone treatment of multiple myeloma. Blood, 80: 887-890, 1992.
    • (1992) Blood , vol.80 , pp. 887-890
    • Alexanian, R.1    Dimopoulos, M.A.2    Delasalle, K.3    Barlogie, B.4
  • 9
  • 11
    • 0033105537 scopus 로고    scopus 로고
    • Cell adhesion mediated drug resistance (CAM-DR): Role of integrins and resistance to apoptosis in human myeloma cell lines
    • Damiano, J. S., Cress, A. E., Hazlehurst, L. A., Shtil, A. A., and Dalton, W. S. Cell adhesion mediated drug resistance (CAM-DR): Role of integrins and resistance to apoptosis in human myeloma cell lines. Blood, 93: 1658-1667, 1999.
    • (1999) Blood , vol.93 , pp. 1658-1667
    • Damiano, J.S.1    Cress, A.E.2    Hazlehurst, L.A.3    Shtil, A.A.4    Dalton, W.S.5
  • 12
    • 0025356050 scopus 로고
    • The role of interleukin-1 and tumour necrosis factor-α in human multiple myeloma
    • Carter, A., Merchav, S., Silvian-Draxler, I., and Tatarsky, I. The role of interleukin-1 and tumour necrosis factor-α in human multiple myeloma. Br. J. Haematol., 74: 424-431, 1990.
    • (1990) Br. J. Haematol. , vol.74 , pp. 424-431
    • Carter, A.1    Merchav, S.2    Silvian-Draxler, I.3    Tatarsky, I.4
  • 14
    • 0030041147 scopus 로고    scopus 로고
    • Multiple myeloma cell adhesion-induced interleukin-6 expression in bone marrow stromal cells involves activation of NF-κ B
    • Chauhan, D., Uchiyama, H., Akbarali, Y., Urashima, M., Yamamoto, K., Libermann, T. A., and Anderson, K. C. Multiple myeloma cell adhesion-induced interleukin-6 expression in bone marrow stromal cells involves activation of NF-κ B. Blood, 87: 1104-1112, 1996.
    • (1996) Blood , vol.87 , pp. 1104-1112
    • Chauhan, D.1    Uchiyama, H.2    Akbarali, Y.3    Urashima, M.4    Yamamoto, K.5    Libermann, T.A.6    Anderson, K.C.7
  • 15
    • 0033377355 scopus 로고    scopus 로고
    • The role of adhesion receptors in the pathogenesis of multiple myeloma
    • Witzig, T. E. The role of adhesion receptors in the pathogenesis of multiple myeloma. Hematol. Oncol. Clin. N. Am., 13: 1127-1143, 1999.
    • (1999) Hematol. Oncol. Clin. N. Am. , vol.13 , pp. 1127-1143
    • Witzig, T.E.1
  • 16
    • 0024503249 scopus 로고
    • Paracrine rather than autocrine regulation of myeloma-cell growth and differentiation by interleukin-6
    • Klein, B., Zhang, X. G., Jourdan, M., Content, J., Houssiau, F., Aarden, L., Piechaczyk, M., and Bataille, R. Paracrine rather than autocrine regulation of myeloma-cell growth and differentiation by interleukin-6. Blood, 73: 517-526, 1989.
    • (1989) Blood , vol.73 , pp. 517-526
    • Klein, B.1    Zhang, X.G.2    Jourdan, M.3    Content, J.4    Houssiau, F.5    Aarden, L.6    Piechaczyk, M.7    Bataille, R.8
  • 18
    • 0026558680 scopus 로고
    • Interleukin-6 dependence of advanced malignant plasma cell dyscrasias
    • Zhang, X. G., Bataille, R., Widjenes, J., and Klein, B. Interleukin-6 dependence of advanced malignant plasma cell dyscrasias. Cancer (Phila.), 69: 1373-1376, 1992.
    • (1992) Cancer (Phila.) , vol.69 , pp. 1373-1376
    • Zhang, X.G.1    Bataille, R.2    Widjenes, J.3    Klein, B.4
  • 19
    • 0029019664 scopus 로고
    • Interleukin-6 inhibits apoptosis of malignant plasma cells
    • Lichtenstein, A., Tu, Y., Fady, C., Vescio, R., and Berenson, J. Interleukin-6 inhibits apoptosis of malignant plasma cells. Cell Immunol., 162: 248-255, 1995.
    • (1995) Cell Immunol. , vol.162 , pp. 248-255
    • Lichtenstein, A.1    Tu, Y.2    Fady, C.3    Vescio, R.4    Berenson, J.5
  • 20
    • 0032168152 scopus 로고    scopus 로고
    • Interleukin-6-type cytokine signalling through the gp130/ Jak/STAT pathway
    • Heinrich, P. C., Behrmann, I., Muller-Newen, G., Schaper, F., and Graeve, L. Interleukin-6-type cytokine signalling through the gp130/ Jak/STAT pathway. Biochem. J., 334: 297-314, 1998.
    • (1998) Biochem. J. , vol.334 , pp. 297-314
    • Heinrich, P.C.1    Behrmann, I.2    Muller-Newen, G.3    Schaper, F.4    Graeve, L.5
  • 21
    • 0033401641 scopus 로고    scopus 로고
    • Mechanisms of myeloma cell growth control
    • Jelinek, D. F. Mechanisms of myeloma cell growth control. Hematol. Oncol. Clin. N. Am., 13: 1145-1157, 1999.
    • (1999) Hematol. Oncol. Clin. N. Am. , vol.13 , pp. 1145-1157
    • Jelinek, D.F.1
  • 22
  • 24
    • 0032711250 scopus 로고    scopus 로고
    • IL-6 up-regulates mcl-1 in human myeloma cells through JAK/STAT rather than ras/MAP kinase pathway
    • Puthier, D., Bataille, R., and Amiot, M. IL-6 up-regulates mcl-1 in human myeloma cells through JAK/STAT rather than ras/MAP kinase pathway. Eur. J. Immunol., 29: 3945-3950, 1999.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 3945-3950
    • Puthier, D.1    Bataille, R.2    Amiot, M.3
  • 29
    • 0029880038 scopus 로고    scopus 로고
    • Role of bcl-X(L) in the control of apoptosis in murine myeloma cells
    • Gauthier, E. R., Piche, L., Lemieux, G., and Lemieux, R. Role of bcl-X(L) in the control of apoptosis in murine myeloma cells. Cancer Res., 56: 1451-1456, 1996.
    • (1996) Cancer Res. , vol.56 , pp. 1451-1456
    • Gauthier, E.R.1    Piche, L.2    Lemieux, G.3    Lemieux, R.4
  • 32
    • 0027480450 scopus 로고
    • MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2
    • Kozopas, K. M., Yang, T., Buchan, H. L., Zhou, P., and Craig, R. W. MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2. Proc. Natl. Acad. Sci. USA, 90: 3516-3520, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3516-3520
    • Kozopas, K.M.1    Yang, T.2    Buchan, H.L.3    Zhou, P.4    Craig, R.W.5
  • 33
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M., and Rogers, S. W. PEST sequences and regulation by proteolysis. Trends Biochem. Sci., 21: 267-271, 1996.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 34
    • 0037085778 scopus 로고    scopus 로고
    • Myeloid cell factor-1 is a critical survival factor for multiple myeloma
    • Zhang, B., Gojo, I., and Fenton, R. G. Myeloid cell factor-1 is a critical survival factor for multiple myeloma. Blood, 99: 1885-1893, 2002.
    • (2002) Blood , vol.99 , pp. 1885-1893
    • Zhang, B.1    Gojo, I.2    Fenton, R.G.3
  • 35
    • 0034661538 scopus 로고    scopus 로고
    • Protein kinase inhibitors flavopiridol and 7-hydroxy-staurosporine down-regulate antiapoptosis proteins in B-cell chronic lymphocytic leukemia
    • Kitada, S., Zapata, J. M., Andreeff, M., and Reed, J. C. Protein kinase inhibitors flavopiridol and 7-hydroxy-staurosporine down-regulate antiapoptosis proteins in B-cell chronic lymphocytic leukemia. Blood, 96: 393-397, 2000.
    • (2000) Blood , vol.96 , pp. 393-397
    • Kitada, S.1    Zapata, J.M.2    Andreeff, M.3    Reed, J.C.4
  • 37
    • 0032189802 scopus 로고    scopus 로고
    • Mcl-1 expression in human neutrophils: Regulation by cytokines and correlation with cell survival
    • Moulding, D. A., Quayle, J. A., Hart, C. A., and Edwards, S. W. Mcl-1 expression in human neutrophils: Regulation by cytokines and correlation with cell survival. Blood, 92: 2495-502, 1998.
    • (1998) Blood , vol.92 , pp. 2495-2502
    • Moulding, D.A.1    Quayle, J.A.2    Hart, C.A.3    Edwards, S.W.4
  • 38
    • 0034283981 scopus 로고    scopus 로고
    • Apoptosis is rapidly triggered by antisense depletion of MCL-1 in differentiating U937 cells
    • Moulding, D. A., Giles, R. V., Spiller, D. G., White, M. R., Tidd, D. M., and Edwards, S. W. Apoptosis is rapidly triggered by antisense depletion of MCL-1 in differentiating U937 cells. Blood, 96: 1756-1763, 2000.
    • (2000) Blood , vol.96 , pp. 1756-1763
    • Moulding, D.A.1    Giles, R.V.2    Spiller, D.G.3    White, M.R.4    Tidd, D.M.5    Edwards, S.W.6
  • 39
    • 0032006805 scopus 로고    scopus 로고
    • Elevated expression of the apoptotic regulator Mcl-1 at the time of leukemic relapse
    • Kaufmann, S. H., Karp, J. E., Svingen, P. A., Krajewski, S., Burke, P. J., Gore, S. D., and Reed, J. C. Elevated expression of the apoptotic regulator Mcl-1 at the time of leukemic relapse. Blood, 91: 991-1000, 1998.
    • (1998) Blood , vol.91 , pp. 991-1000
    • Kaufmann, S.H.1    Karp, J.E.2    Svingen, P.A.3    Krajewski, S.4    Burke, P.J.5    Gore, S.D.6    Reed, J.C.7
  • 40
    • 0035055595 scopus 로고    scopus 로고
    • Mechanisms of action of flavopiridol
    • Sedlacek, H. H. Mechanisms of action of flavopiridol. Crit. Rev. Oncol.-Hematol., 38: 139-170, 2001.
    • (2001) Crit. Rev. Oncol.-Hematol. , vol.38 , pp. 139-170
    • Sedlacek, H.H.1
  • 41
    • 0033375469 scopus 로고    scopus 로고
    • Flavopiridol: The first cyclin-dependent kinase inhibitor in human clinical trials
    • Senderowicz, A. M. Flavopiridol: The first cyclin-dependent kinase inhibitor in human clinical trials. Investig. New Drugs, 17: 313-320, 1999.
    • (1999) Investig. New Drugs , vol.17 , pp. 313-320
    • Senderowicz, A.M.1
  • 42
    • 0034162636 scopus 로고    scopus 로고
    • Preclinical and clinical development of cyclin-dependent kinase modulators
    • Senderowicz, A. M., and Sausville, E. A. Preclinical and clinical development of cyclin-dependent kinase modulators. J. Natl. Cancer Inst., 92: 376-387, 2000.
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 376-387
    • Senderowicz, A.M.1    Sausville, E.A.2
  • 43
    • 0027433237 scopus 로고
    • Alteration of the phosphorylation state of p34cdc2 kinase by the flavone L86-8275 in breast carcinoma cells. Correlation with decreased HI kinase activity
    • Worland, P. J., Kaur, G., Stetler-Stevenson, M., Sebers, S., Sartor, O., and Sausville, E. A. Alteration of the phosphorylation state of p34cdc2 kinase by the flavone L86-8275 in breast carcinoma cells. Correlation with decreased HI kinase activity. Biochem. Pharmacol., 46: 1831-1840, 1993.
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 1831-1840
    • Worland, P.J.1    Kaur, G.2    Stetler-Stevenson, M.3    Sebers, S.4    Sartor, O.5    Sausville, E.A.6
  • 46
    • 0036220822 scopus 로고    scopus 로고
    • Complexities in the development of cyclin-dependent kinase inhibitor drugs
    • Sausville, E. A. Complexities in the development of cyclin-dependent kinase inhibitor drugs. Trends Mol. Med. 8: S32-S37, 2002.
    • (2002) Trends Mol. Med. , vol.8
    • Sausville, E.A.1
  • 48
    • 0032004973 scopus 로고    scopus 로고
    • The role of Cdk7 in CAK function, a retro-retrospective
    • Harper, J. W., and Elledge, S. J. The role of Cdk7 in CAK function, a retro-retrospective. Genes Dev., 12: 285-289, 1998.
    • (1998) Genes Dev. , vol.12 , pp. 285-289
    • Harper, J.W.1    Elledge, S.J.2
  • 49
    • 0031840672 scopus 로고    scopus 로고
    • Molecular genetics of the RNA polymerase 11 general transcriptional machinery
    • Hampsey, M. Molecular genetics of the RNA polymerase 11 general transcriptional machinery. Microbiol. Mol. Biol. Rev., 62: 465-503, 1998.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 465-503
    • Hampsey, M.1
  • 50
    • 0034111019 scopus 로고    scopus 로고
    • P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II
    • Price, D. H. P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II. Mol. Cell. Biol., 20: 2629-2634, 2000.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2629-2634
    • Price, D.H.1
  • 52
    • 0035943710 scopus 로고    scopus 로고
    • Flavopiridol inactivates P-TEFb and blocks most RNA polymerase II transcription in vivo
    • Chao, S. H., and Price, D. H. Flavopiridol inactivates P-TEFb and blocks most RNA polymerase II transcription in vivo. J. Biol. Chem., 276: 31793-31793-31799, 2001.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31793-31793
    • Chao, S.H.1    Price, D.H.2
  • 53
    • 0035141075 scopus 로고    scopus 로고
    • Development of cyclin-dependent kinase modulators as novel therapeutic approaches for hematological malignancies
    • Senderowicz, A. M. Development of cyclin-dependent kinase modulators as novel therapeutic approaches for hematological malignancies. Leukemia (Baltimore), 15: 1-9, 2001.
    • (2001) Leukemia (Baltimore) , vol.15 , pp. 1-9
    • Senderowicz, A.M.1
  • 54
    • 0034917456 scopus 로고    scopus 로고
    • The cyclin-dependent kinase inhibitor flavopiridol induces apoptosis in human leukemia cells (U937) through the mitochondrial rather than the receptor-mediated pathway
    • Decker, R. H., Dai, Y., and Grant, S. The cyclin-dependent kinase inhibitor flavopiridol induces apoptosis in human leukemia cells (U937) through the mitochondrial rather than the receptor-mediated pathway. Cell Death Differ., 8: 715-724, 2001.
    • (2001) Cell Death Differ. , vol.8 , pp. 715-724
    • Decker, R.H.1    Dai, Y.2    Grant, S.3
  • 55
    • 0035866782 scopus 로고    scopus 로고
    • The cyclin-dependent kinase inhibitor (CDKI) flavopiridol disrupts phorbol 12-myristate 13-acetate-induced differentiation and CDKI expression while enhancing apoptosis in human myeloid leukemia cells
    • Cartee, L., Wang, Z., Decker, R. H., Chellappan, S. P., Fusaro, G., Hirsch, K. G., Sankala, H. M., Dent, P., and Grant, S. The cyclin-dependent kinase inhibitor (CDKI) flavopiridol disrupts phorbol 12-myristate 13-acetate-induced differentiation and CDKI expression while enhancing apoptosis in human myeloid leukemia cells. Cancer Res., 61: 2583-2591, 2001.
    • (2001) Cancer Res. , vol.61 , pp. 2583-2591
    • Cartee, L.1    Wang, Z.2    Decker, R.H.3    Chellappan, S.P.4    Fusaro, G.5    Hirsch, K.G.6    Sankala, H.M.7    Dent, P.8    Grant, S.9
  • 56
    • 0034935026 scopus 로고    scopus 로고
    • Flavopiridol circumvents Bcl-2 family mediated inhibition of apoptosis and drug resistance in B-cell chronic lymphocytic leukaemia
    • Pepper, C., Thomas, A., Hoy, T., Fegan, C., and Bentley, P. Flavopiridol circumvents Bcl-2 family mediated inhibition of apoptosis and drug resistance in B-cell chronic lymphocytic leukaemia. Br. J. Haematol., 114: 70-77, 2001.
    • (2001) Br. J. Haematol. , vol.114 , pp. 70-77
    • Pepper, C.1    Thomas, A.2    Hoy, T.3    Fegan, C.4    Bentley, P.5
  • 58
    • 0033121314 scopus 로고    scopus 로고
    • Role of NF-κB in the rescue of multiple myeloma cells from glucocorticoid-induced apoptosis by bcl-2
    • Feinman, R., Koury, J., Thames, M., Barlogie, B., Epstein, J., and Siegel, D. S. Role of NF-κB in the rescue of multiple myeloma cells from glucocorticoid-induced apoptosis by bcl-2. Blood, 93: 3044-3052, 1999.
    • (1999) Blood , vol.93 , pp. 3044-3052
    • Feinman, R.1    Koury, J.2    Thames, M.3    Barlogie, B.4    Epstein, J.5    Siegel, D.S.6
  • 59
    • 0032409781 scopus 로고    scopus 로고
    • Bcl-2 family proteins
    • Reed, J. C. Bcl-2 family proteins. Oncogene, 17: 3225-3236, 1998.
    • (1998) Oncogene , vol.17 , pp. 3225-3236
    • Reed, J.C.1
  • 60
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross, A., McDonnell, J. M., and Korsmeyer, S. J. BCL-2 family members and the mitochondria in apoptosis. Genes Dev., 13: 1899-911, 1999.
    • (1999) Genes Dev. , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 61
    • 0030916209 scopus 로고    scopus 로고
    • Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway
    • Diehl, J. A., Zindy, F., and Sherr, C. J. Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway. Genes Dev., 11: 957-972, 1997.
    • (1997) Genes Dev. , vol.11 , pp. 957-972
    • Diehl, J.A.1    Zindy, F.2    Sherr, C.J.3
  • 62
    • 0029760928 scopus 로고    scopus 로고
    • Reversible phosphorylation of the C-terminal domain of RNA polymerase II
    • Dahmus, M. E. Reversible phosphorylation of the C-terminal domain of RNA polymerase II. J. Biol. Chem., 271: 19009-19012, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19009-19012
    • Dahmus, M.E.1
  • 63
    • 0033522915 scopus 로고    scopus 로고
    • The transcriptional inhibitors, actinomycin D and α-amanitin, activate the HIV-1 promoter and favor phosphorylation of the RNA polymerase II C-terminal domain
    • Casse, C., Giannoni, F., Nguyen, V. T., Dubois, M. F., and Bensaude, O. The transcriptional inhibitors, actinomycin D and α-amanitin, activate the HIV-1 promoter and favor phosphorylation of the RNA polymerase II C-terminal domain. J. Biol. Chem., 274: 16097-16106, 1999.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16097-16106
    • Casse, C.1    Giannoni, F.2    Nguyen, V.T.3    Dubois, M.F.4    Bensaude, O.5
  • 64
    • 0028787404 scopus 로고
    • The transcriptional elongation inhibitor 5, 6-dichloro-1-β-D-ribofuranosylbenzimidazole inhibits transcription factor IIH-associated protein kinase
    • Yankulov, K., Yamashita, K., Roy, R., Egly, J. M., and Bentley, D. L. The transcriptional elongation inhibitor 5, 6-dichloro-1-β-D-ribofuranosylbenzimidazole inhibits transcription factor IIH-associated protein kinase. J. Biol. Chem., 270: 23922-23925, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23922-23925
    • Yankulov, K.1    Yamashita, K.2    Roy, R.3    Egly, J.M.4    Bentley, D.L.5
  • 65
    • 0019902611 scopus 로고
    • Mechanism of action of dichloro-β-D-ribofuranosylbenzimidazole: Effect on in vitro transcription
    • Zandomeni, R., Mittleman, B., Bunick, D., Ackerman, S., and Weinmann, R. Mechanism of action of dichloro-β-D-ribofuranosylbenzimidazole: Effect on in vitro transcription. Proc. Natl. Acad. Sci. USA, 79: 3167-3170, 1982.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3167-3170
    • Zandomeni, R.1    Mittleman, B.2    Bunick, D.3    Ackerman, S.4    Weinmann, R.5
  • 67
    • 0030878058 scopus 로고    scopus 로고
    • Modulation by (iso)flavonoids of the ATPase activity of the multidrug resistance protein
    • Hooijberg, J. H., Broxterman, H. J., Heijn, M., Fles, D. L., Lankelma, J., and Pinedo, H. M. Modulation by (iso)flavonoids of the ATPase activity of the multidrug resistance protein. FEBS Lett., 413: 344-348, 1997.
    • (1997) FEBS Lett. , vol.413 , pp. 344-348
    • Hooijberg, J.H.1    Broxterman, H.J.2    Heijn, M.3    Fles, D.L.4    Lankelma, J.5    Pinedo, H.M.6
  • 69
    • 0036138680 scopus 로고    scopus 로고
    • Growth inhibition and apoptosis of myeloma cells by the CDK inhibitor flavopiridol
    • Semenov, I., Akyuz, C., Roginskaya, V., Chauhan, D., and Corey, S. J. Growth inhibition and apoptosis of myeloma cells by the CDK inhibitor flavopiridol. Leuk. Res., 26: 271-280, 2002.
    • (2002) Leuk. Res. , vol.26 , pp. 271-280
    • Semenov, I.1    Akyuz, C.2    Roginskaya, V.3    Chauhan, D.4    Corey, S.J.5
  • 70
    • 0031876318 scopus 로고    scopus 로고
    • mcl-1 is an immediate-early gene activated by the granulocyte-macrophage colony-stimulating factor (GM-CSF) signaling pathway and is one component of the GM-CSF viability response
    • Chao, J. R., Wang, J. M., Lee, S. F., Peng, H. W., Lin, Y. H., Chou, C. H., Li, J. C., Huang, H. M., Chou, C. K., Kuo, M. L., Yen, J. J., and Yang-Yen, H. F. mcl-1 is an immediate-early gene activated by the granulocyte-macrophage colony-stimulating factor (GM-CSF) signaling pathway and is one component of the GM-CSF viability response. Mol. Cell. Biol., 18: 4883-4898, 1998.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4883-4898
    • Chao, J.R.1    Wang, J.M.2    Lee, S.F.3    Peng, H.W.4    Lin, Y.H.5    Chou, C.H.6    Li, J.C.7    Huang, H.M.8    Chou, C.K.9    Kuo, M.L.10    Yen, J.J.11    Yang-Yen, H.F.12
  • 71
    • 0032533599 scopus 로고    scopus 로고
    • Flavopiridol induces apoptosis in chronic lymphocytic leukemia cells via activation of caspase-3 without evidence of bcl-2 modulation or dependence on functional p53
    • Byrd, J. C., Shinn, C., Waselenko, J. K., Fuchs, E. J., Lehman, T. A., Nguyen, P. L., Flinn, I. W., Diehl, L. F., Sausville, E., and Grever, M. R. Flavopiridol induces apoptosis in chronic lymphocytic leukemia cells via activation of caspase-3 without evidence of bcl-2 modulation or dependence on functional p53. Blood, 92: 3804-3816, 1998.
    • (1998) Blood , vol.92 , pp. 3804-3816
    • Byrd, J.C.1    Shinn, C.2    Waselenko, J.K.3    Fuchs, E.J.4    Lehman, T.A.5    Nguyen, P.L.6    Flinn, I.W.7    Diehl, L.F.8    Sausville, E.9    Grever, M.R.10
  • 72
    • 0040932434 scopus 로고    scopus 로고
    • The novel cyclin-dependent kinase inhibitor flavopiridol downregulates Bcl-2 and induces growth arrest and apoptosis in chronic B-cell leukemia lines
    • Konig, A., Schwartz, G. K., Mohammad, R. M., Al-Katib, A., and Gabrilove, J. L. The novel cyclin-dependent kinase inhibitor flavopiridol downregulates Bcl-2 and induces growth arrest and apoptosis in chronic B-cell leukemia lines. Blood, 90: 4307-4312, 1997.
    • (1997) Blood , vol.90 , pp. 4307-4312
    • Konig, A.1    Schwartz, G.K.2    Mohammad, R.M.3    Al-Katib, A.4    Gabrilove, J.L.5
  • 73
    • 0034644659 scopus 로고    scopus 로고
    • Bcl-2 independence of flavopiridol-induced apoptosis. Mitochondrial depolarization in the absence of cytochrome c release
    • Achenbach, T. V., Muller, R., and Slater, E. P. Bcl-2 independence of flavopiridol-induced apoptosis. Mitochondrial depolarization in the absence of cytochrome c release. J. Biol. Chem., 275: 32089-32097, 2000.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32089-32097
    • Achenbach, T.V.1    Muller, R.2    Slater, E.P.3
  • 74
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Deveraux, Q. L., Takahashi, R., Salvesen, G. S., and Reed, J. C. X-linked IAP is a direct inhibitor of cell-death proteases. Nature (Lond.), 388: 300-304, 1997.
    • (1997) Nature (Lond.) , vol.388 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 75
    • 0033082995 scopus 로고    scopus 로고
    • IAP family proteins-suppressors of apoptosis
    • Deveraux, Q. L., and Reed, J. C. IAP family proteins-suppressors of apoptosis. Genes Dev., 13: 239-252, 1999.
    • (1999) Genes Dev. , vol.13 , pp. 239-252
    • Deveraux, Q.L.1    Reed, J.C.2
  • 77
    • 0032476668 scopus 로고    scopus 로고
    • Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • Jaattela, M., Wissing, D., Kokholm, K., Kallunki, T., and Egeblad, M. Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J., 17: 6124-6134, 1998.
    • (1998) EMBO J. , vol.17 , pp. 6124-6134
    • Jaattela, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egeblad, M.5
  • 78
    • 0029904810 scopus 로고    scopus 로고
    • Flavopiridol: A cytotoxic flavone that induces cell death in noncycling A549 human lung carcinoma cells
    • Bible, K. C., and Kaufmann, S. H. Flavopiridol: A cytotoxic flavone that induces cell death in noncycling A549 human lung carcinoma cells. Cancer Res., 56: 4856-4861, 1996.
    • (1996) Cancer Res. , vol.56 , pp. 4856-4861
    • Bible, K.C.1    Kaufmann, S.H.2
  • 80
    • 0029011873 scopus 로고
    • Purification of P-TEFb, a transcription factor required for the transition into productive elongation
    • Marshall, N. F., and Price, D. H. Purification of P-TEFb, a transcription factor required for the transition into productive elongation. J. Biol. Chem., 270: 12335-12338, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12335-12338
    • Marshall, N.F.1    Price, D.H.2
  • 81
    • 0029959881 scopus 로고    scopus 로고
    • Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase
    • Marshall, N. F., Peng, J., Xie, Z., and Price, D. H. Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase. J. Biol. Chem., 271: 27176-27183, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27176-27183
    • Marshall, N.F.1    Peng, J.2    Xie, Z.3    Price, D.H.4
  • 82
    • 0035891288 scopus 로고    scopus 로고
    • 7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes
    • Nguyen, V. T., Kiss, T., Michels, A. A., and Bensaude, O. 7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes. Nature (Lond.), 414: 322-325, 2001.
    • (2001) Nature (Lond.) , vol.414 , pp. 322-325
    • Nguyen, V.T.1    Kiss, T.2    Michels, A.A.3    Bensaude, O.4
  • 83
    • 0035891271 scopus 로고    scopus 로고
    • The 7SK small nuclear RNA inhibits the CDK9/cyclin T1 kinase to control transcription
    • Yang, Z., Zhu, Q., Luo, K., and Zhou, Q. The 7SK small nuclear RNA inhibits the CDK9/cyclin T1 kinase to control transcription. Nature (Lond.), 414: 317-322, 2001.
    • (2001) Nature (Lond.) , vol.414 , pp. 317-322
    • Yang, Z.1    Zhu, Q.2    Luo, K.3    Zhou, Q.4
  • 85
    • 0034669945 scopus 로고    scopus 로고
    • Loss of PTEN expression leading to high Akt activation in human multiple myelomas
    • Hyun, T., Yam, A., Pece, S., Xie, X., Zhang. J., Miki, T., Gutkind, J. S., and Li, W. Loss of PTEN expression leading to high Akt activation in human multiple myelomas. Blood, 96: 3560-3568, 2000.
    • (2000) Blood , vol.96 , pp. 3560-3568
    • Hyun, T.1    Yam, A.2    Pece, S.3    Xie, X.4    Zhang, J.5    Miki, T.6    Gutkind, J.S.7    Li, W.8
  • 86
    • 0034710535 scopus 로고    scopus 로고
    • Expression of PTEN in PTEN-deficient multiple myeloma cells abolishes tumor growth in vivo
    • Ge, N. L., and Rudikoff, S. Expression of PTEN in PTEN-deficient multiple myeloma cells abolishes tumor growth in vivo. Oncogene, 19: 4091-4095, 2000.
    • (2000) Oncogene , vol.19 , pp. 4091-4095
    • Ge, N.L.1    Rudikoff, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.